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J. Biol. Chem., Vol. 279, Issue 18, 18903-18910, April 30, 2004

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The Three-dimensional Structure of Invertase (-Fructosidase) from Thermotoga maritima Reveals a Bimodular Arrangement and an Evolutionary Relationship between Retaining and Inverting Glycosidases^*

François Alberto, Christophe Bignon, Gerlind Sulzenbacher, Bernard Henrissat, and Mirjam Czjzek

From the Architecture et Fonction des Macromolécules Biologiques, CNRS and Université Aix-Marseille I & II, Institut de Biologie Structurale et Microbiologie, 31 Chemin Joseph Aiguier, 13402 Marseille cedex 20, France

Thermotoga maritima invertase (-fructosidase) hydrolyzes sucrose to release fructose and glucose, which are major carbon and energy sources for both prokaryotes and eukaryotes. The name "invertase" was given to this enzyme over a century ago, because the 1:1 mixture of glucose and fructose that it produces was named "invert sugar." Despite its name, the enzyme operates with a mechanism leading to the retention of the anomeric configuration at the site of cleavage. The enzyme belongs to family GH32 of the sequence-based classification of glycosidases. The crystal structure, determined at 2-Å resolution, reveals two modules, namely a five-bladed -propeller with structural similarity to the -propeller structures of glycosidase from families GH43 and GH68 connected to a -sandwich module. Three carboxylates at the bottom of a deep, negatively charged funnel-shaped depression of the -propeller are essential for catalysis and function as nucleophile, general acid, and transition state stabilizer, respectively. The catalytic machinery of invertase is perfectly superimposable to that of the enzymes of families GH43 and GH68. The variation in the position of the furanose ring at the site of cleavage explains the different mechanisms evident in families GH32 and GH68 (retaining) and GH43 (inverting) furanosidases.

Received for publication, December 19, 2003 , and in revised form, February 5, 2004.

The atomic coordinates and structure factors (code 1UYP) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^* This work was partly funded by grant QLK5-CT-2001-00443 (EDEN) from the European Commission. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed. Tel.: 33-491-164-513; Fax: 33-491-164-536; E-mail: czjzek{at}afmb.cnrs-mrs.fr.

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